In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATP

FEBS Letters

Lissin, Nikolai M.¹ 

[1] Centre de Biochimie et Biologie Moléculaire, Centre National de la Recherche Scientifique, 31 Chemin Joseph Aiguier, 13402 Marseille, Cédex 20, France

关键词: Chaperonin;    Cpn60;    GroEL;    Self-assembly;    Mg-ATP;    Protein folding;    SDS;    sodium dodecyl sulphate;    PAGE;    polyacrylamide gel-electrophoresis;    EDTA;    ethylenediaminetetraacetic acid;    DTT;    dithiothreitol;    ATP-γ-S;    adenosine 5′-O-(3-thiotriphosphate);   

DOI  :  10.1016/0014-5793(95)00151-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg²⁺ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg²⁺ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

【 授权许可】

Unknown